ID   A0A0G2HXJ0_9PEZI        Unreviewed;      1172 AA.
AC   A0A0G2HXJ0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Putative phosphoribosyl transferase domain protein {ECO:0000313|EMBL:KKY32675.1};
GN   ORFNames=UCDDA912_g07381 {ECO:0000313|EMBL:KKY32675.1};
OS   Diaporthe ampelina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX   NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY32675.1, ECO:0000313|Proteomes:UP000034680};
RN   [1] {ECO:0000313|EMBL:KKY32675.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY32675.1};
RA   Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT   "Distinctive expansion of gene families associated with plant cell wall
RT   degradation and secondary metabolism in the genomes of grapevine trunk
RT   pathogens.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KKY32675.1, ECO:0000313|Proteomes:UP000034680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DA912 {ECO:0000313|EMBL:KKY32675.1};
RA   Morales-Cruz A., Amrine K.C., Cantu D.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY32675.1}.
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DR   EMBL; LCUC01000292; KKY32675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2HXJ0; -.
DR   STRING; 1214573.A0A0G2HXJ0; -.
DR   OrthoDB; 1608525at2759; -.
DR   UniPathway; UPA00057; UER00099.
DR   Proteomes; UP000034680; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:InterPro.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:InterPro.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005919; Pmev_kin_anim.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF25; PHOSPHOMEVALONATE KINASE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF04275; P-mevalo_kinase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW   Transferase {ECO:0000313|EMBL:KKY32675.1}.
FT   DOMAIN          317..507
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          916..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..940
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1172 AA;  127651 MW;  932C4E2FCE27BF54 CRC64;
     MATVDSLKRA LRQTAEEATL IIPRQPFSDA QYSAGLDILT HGAGWLNYED FIIPQTSQLL
     GPLFDSRTHV SVLEIGPGRR SLLSYLPRHL RHKVRKYKAF EPNSLFAARL EESLAGDPGS
     ERGPTLPCLE SPPDICRKPF DANDNKGSGT RTNISSRDNG DKYDVILVCH SMYGMKPKRA
     FIGRMLGMLA DDCMWPHVGG LLVVFHRDNG ALHLEDLVCH RTASFCAGVV EVADNDGQLD
     SFASFVAGFT ADDAIRAEWR KICRALGRRG KDRPDHLLFS SPELMVAFTR HAVKIQELAG
     LYPVLKGRRM IKNHEATLHH PAPVVKPTEI RHVQTCVGWA LENHVGLTVV GGGHSGQSCW
     PNVLSVDMSA FDEIHIFSDE CMEDVGFPPL VVAEAGCISG NIIRDTKEAG LTVPLGARPS
     VGAGLWLQGG IGHQSRLHGL ACDAIVGAVI VSVKDPSQIL CVGNVPAEAQ PVDAVRPQNE
     AEVLWAIKGA GTNFGIVISV VFQAYAVPTY RTRNWVVRLG NNSDAQQKII DFDKIVTSYL
     PRNCSADAYL HWENGQLQLG VTLFESLKDE PTSSLKTAMA MMDSSWGPSD GPEVMDGVGL
     FDAEMYVSRL HGGHAGGRTS SFKRCVFLKH IGEAEVARRL VAAIDSRPSP FCYLHLLQGG
     GAVRDVAAHV TAFGCRDWDF ACVITGVWPR DQDDTEFARC VSQWVYGIAE DLLTLSHCCG
     AYGADLGPGS RDSVLATQAF GPNRQRLARL KHIMDPRDVL AYACPLPKVS LEQKIIVLVT
     GESCAGKDFC ADVWASVMTR CNTTRHAQLN ARVVSISSAT KREYAAATGA DIGRLLWDRD
     YKEEHRPALT AFFKEQTRER PELPKEQFLS VVRGAADVDV LLITGMRDEA PLAAYSHLVP
     ESRLLEVYVH AGEEKRRRRG GRGNAVEGSN KTSHNNGSEP DTIALSYSPS LIFHNDMGGS
     ESAEKFAKQR LLPFLHNDLW HLASMVSTAP EFPRPGIDFH HVLGIPQQPG GLALCASLLR
     THFAGDWAKV DSVACCEAGG FIFAPVLALQ VNLPLLLIRD AGKLPPPTVS VAKHRSYVSS
     VVSDDALQGR IELELDRVPK GAGGTVVVVD DVLSTGETLC AVLLLLGKAG VRAENVSVMI
     VAEFPLHRGR ELLRQRGFGR TSVQSLLVFD GA
//